IMPACT OF pH, TEMPERATURE AND GAMMA RADIATION ON G6PD ACTIVITY AND ERYTHROCYTE MORPHOLOGY IN G6PD DEFICIENCY
Keywords:
Radiation effect, G6PD, erythrocytes, pH, enzymes.Abstract
Glucose-6-Phosphate dehydrogenase (G6PD) deficiency is a genetic condition that primarily affects erythrocytes. G6PD is an enzyme predominantly found in erythrocytes, where it catalyses the oxidation of glucose-6-phosphate in glucose metabolism. Erythrocytes are blood cells produced by stem cells in the bone marrow. Previous research on G6PD deficiency has mainly focused on affected patients. Therefore, the objectives of this study are to optimise the effects of pH and temperature on G6PD enzyme activity, investigate the impact of G6PD deficiency on erythrocytes, and examine the morphology of both normal and G6PD-deficient erythrocytes after exposure to gamma radiation. For the methodology, the dilution method was employed to identify the optimal parameters for G6PD activity. Erythrocytes were obtained from both G6PD-deficient patients and healthy individuals. To study the reactions, substances such as uncoated aspirin and broad bean solutions were added to the erythrocytes. The erythrocytes’ morphology was then examined after exposure to gamma radiation from Cesium-137 for a week. After one week, the samples were observed under a Nikon Eclipse LV/UDM microscope. The results from this irradiation serve as evidence of the effects of G6PD deficiency on erythrocytes and highlight substances that may contribute to the deficiency.
References
Allahverdiyev, A. M., Bagirova, M., Koc, R. C., Ates, S. C., Baydar, S. Y., Yaman, S., Abamor, E. S., & Oztel, O. N. (2012). Glucose-6-phosphate dehydrogenase deficiency and malaria: A method to detect primaquine-induced hemolysis in vitro. https://doi.org/10.5772/48403
Beutler, E., & Duparc, S. (2007). Glucose-6-phosphate dehydrogenase deficiency and antimalarial drug development. American Journal of Tropical Medicine and Hygiene, 77(4), 779–789.
Bonilla, J. F., Sanchez, M. C., & Chuaire, L. (2007). Glucose-6-phosphate dehydrogenase (G6PD): Response of the human erythrocyte and another cells to the decrease in their activity. Colombia Médica, 38(1).
Carter, N., Pamba, A., Duparc, S., & Waitumbi, J. N. (2011). Frequency of glucose-6-phosphate dehydrogenase deficiency in malaria patients from six African countries enrolled in two randomized anti-malarial clinical trials. Malaria Journal, 10, Article 241. https://doi.org/10.1186/1475-2875-10-241
Felix, K., Rockwood, L. D., Pretsch, W., Nair, J., Bartsch, H., Bornkamm, G. W., & Janz, S. (2002). Moderate G6PD deficiency increases mutation rates in the brain of mice. Free Radical Biology and Medicine, 32, 663–673.
Fernando, N., Fernando, K., Williams, S., & Premawardhena, A. (2024). A case report of acute oxidative haemolysis following medicinal plant ingestion in a patient with G6PD deficiency. Clinica Chimica Acta, 558, Article 119624.
Filosa, S., Fico, A., Paglialunga, F., Balestrieri, M., Crooke, A., Verde, P., Abrescia, P., Bautista, J. M., & Martini, G. (2003). Failure to increase glucose consumption through the pentose-phosphate pathway results in the death of glucose-6-phosphate dehydrogenase gene-deleted mouse embryonic stem cells subjected to oxidative stress. Biochemical Journal, 370, 935–943.
Frank, J. E. (2005). Diagnosis and management of G6PD deficiency. American Family Physician, 72(7), 1277.
Garcia, A. A., Mathews, I. I., Horikoshi, N., Matsui, T., Kaur, M., Wakatsuki, S., & Mochly-Rosen, D. (2022). Stabilization of glucose-6-phosphate dehydrogenase oligomers enhances catalytic activity and stability of clinical variants. Journal of Biological Chemistry, 298(3), Article 101610. https://doi.org/10.1016/j.jbc.2022.101610
Haeussler, K., Berneburg, I., Jortzik, E., Hahn, J., Rahbari, M., Schulz, N., Preuss, J., Zapol'skii, V. A., Bode, L., Pinkerton, A. B., Kaufmann, D. E., Rahlfs, S., & Becker, K. (2019). Glucose 6-phosphate dehydrogenase 6-phosphogluconolactonase: Characterization of the Plasmodium vivax enzyme and inhibitor studies. Malaria Journal, 18(1), Article 22. https://doi.org/10.1186/s12936-019-2651-z
Israel, A., Raz, I., Green, I., Golan-Cohen, A., Berkovitch, M., Magen, E., Vinker, S., & Merzon, E. (2025). Health disparities in diabetes treatment: The challenge of G6PD deficiency. Diabetes Research and Clinical Practice, 219, Article 111965.
Karadsheh, N. S., Quttaineh, N. A., Karadsheh, S. N., & El-Khateeb, M. (2021). Effect of combined G6PD deficiency and diabetes on protein oxidation and lipid peroxidation. BMC Endocrine Disorders, 21(1), Article 246. https://doi.org/10.1186/s12902-021-00911-6
Koehler, A., & Van Noorden, C. J. (2003). Reduced nicotinamide adenine dinucleotide phosphate and the higher incidence of pollution-induced liver cancer in female flounder. Environmental Toxicology and Chemistry, 22, 2703–2710.
Kotaka, M., Gover, S., Vandeputte-Rutten, L., Au, S. W. N., Lam, V. M. S., & Adams, M. J. (2005). Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase. Acta Crystallographica Section D: Biological Crystallography, 61, 495–504.
Langer, A. L. (2024). Oxidative hemolysis due to phenazopyridine in the absence of G6PD deficiency. Blood, 144(20), 2155.
Milanowski, P., Carter, T. J., & Weber, G. F. (2013). Enzyme catalysis and the outcome of biochemical reactions. Journal of Proteomics and Bioinformatics, 6, 132–141.
Möller, M. N., Orrico, F., Villar, S. F., López, A. C., Silva, N., Donzé, M., Thomson, L., & Denicola, A. (2022). Oxidants and antioxidants in the redox biochemistry of human red blood cells. ACS Omega, 8(1), 147–168. https://doi.org/10.1021/acsomega.2c06768
Nigam, P. S. (2013). Microbial enzymes with special characteristics for biotechnological applications. Biomolecules, 3, 597–611.
Noori-Daloii, M., Najafi, L., Ganji, S. M., Hajebrahimi, Z., & Sanati, M. (2004). Molecular identification of mutations in G6PD gene in patients with favism in Iran. Journal of Physiology and Biochemistry, 60(4), 273–277.
Oka, S., Hsu, C. P., & Sadoshima, J. (2012). Regulation of cell survival and death by pyridine nucleotides. Circulation Research, 111(5), 611–627. https://doi.org/10.1161/CIRCRESAHA.111.247932
Oliveira, F. A., Silva, D. J. H., Leite, G. L. D., Jham, G. N., & Picanço, M. C. (2009). Resistance of 57 greenhouse-grown accessions of Lycopersicon esculentum and three cultivars to Tuta absoluta (Meyrick) (Lepidoptera: Gelechiidae). Scientia Horticulturae, 119, 182–187. https://doi.org/10.1016/j.scienta.2008.07.012
Park, Y. J., Choe, S. S., Sohn, J. H., & Kim, J. B. (2017). The role of glucose-6-phosphate dehydrogenase in adipose tissue inflammation in obesity. Adipocyte, 6(2), 147–153. https://doi.org/10.1080/21623945.2017.1288321
Peters, A. L., & Van Noorden, C. J. (2009). Glucose-6-phosphate dehydrogenase deficiency and malaria: Cytochemical detection of heterozygous G6PD deficiency in women. Journal of Histochemistry and Cytochemistry, 57(11), 1003–1011.
Prashanth, G. P., & Ismail, S. K. (2025). Community, culture, and chromosomes: Humanistic approach to childhood G6PD deficiency management. Patient Education and Counseling, 131, Article 108570.
Reclos, G., Hatzidakis, C., & Schulpis, K. (2000). Glucose-6-phosphate dehydrogenase deficiency neonatal screening: Preliminary evidence that a high percentage of partially deficient female neonates are missed during routine screening. Journal of Medical Screening, 7(1), 46–51.
Singh, S., Anand, A., & Srivastava, P. K. (2012). Regulation and properties of glucose-6-phosphate dehydrogenase: A review. International Journal of Plant Physiology and Biochemistry, 4(1), 1–19.
Solomon, E., Berg, L., & Martin, D. W. (2010). Biology (9th ed.). Cengage Learning.
Spinelli, S., Marino, A., Remigante, A., & Morabito, R. (2025). Redox homeostasis in red blood cells: From molecular mechanisms to antioxidant strategies. Current Issues in Molecular Biology, 47(8), Article 655. https://doi.org/10.3390/cimb47080655
Sulaiman, A. M., Saghir, S. A. M., Al-Hassan, F. M., Yusoff, N. M., & Zaki, A. H. A. (2013). Molecular characterization of glucose-6-phosphate dehydrogenase deficiency in a university community in Malaysia. Tropical Journal of Pharmaceutical Research, 12(3), 363–368.
Thakor, P., Siddiqui, M. Q., & Patel, T. R. (2024). Analysis of the interlink between glucose-6-phosphate dehydrogenase (G6PD) and lung cancer through multi-omics databases. Heliyon, 10(15), Article e35158.
Tiwari, M. (2017). Glucose 6 phosphate dehydrogenase (G6PD) and neurodegenerative disorders: Mapping diagnostic and therapeutic opportunities. Genes & Diseases, 4(4), 196–203. https://doi.org/10.1016/j.gendis.2017.09.001
Turner, N. J. (2000). Applications of transketolases in organic synthesis. Current Opinion in Biotechnology, 11, 527–531.
Verrelli, B. C., McDonald, J. H., Argyropoulos, G., Destro-Bisol, G., Froment, A., Drousiotou, A., Lefranc, G., Helal, A. N., Loiselet, J., & Tishkoff, S. A. (2002). Evidence for balancing selection from nucleotide sequence analyses of human G6PD. American Journal of Human Genetics, 71, 1112–1128.
Wang, X. T., Au, S. W. N., Lam, V. M. S., & Engel, P. C. (2002). Recombinant human glucose-6-phosphate dehydrogenase: Evidence from an allelic variant for the existence of a critical histidine at the subunit interface. European Journal of Biochemistry, 269, 3417–3424.
Xu, Y., Zhang, Z., Hu, J., Stillman, I. E., Leopold, J. A., Handy, D. E., Loscalzo, J., & Stanton, R. C. (2010). Glucose-6-phosphate dehydrogenase-deficient mice have increased renal oxidative stress and increased albuminuria. FASEB Journal, 24(2), 609–616. https://doi.org/10.1096/fj.09-1357
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